. Cell heredity. Cytogenetics. MECHANISMS OF GENE ACTION 287 come apart after cleavage of the peptide bond hut remain associated, and the enzyme remains fully active. By mild acid treatment, the parts can be separated, and both of the fragments are enzymatically inactive. If these fragments are then mixed, they recombine in equimolar amounts to reconstitute the active enzyme. It is possible that some genetic con- trol devices of the cell employ analogous mechanisms, in which the addi- tion or removal of a short peptide sequence determines enzyme activity. Only isolation and analysis of the enz
. Cell heredity. Cytogenetics. MECHANISMS OF GENE ACTION 287 come apart after cleavage of the peptide bond hut remain associated, and the enzyme remains fully active. By mild acid treatment, the parts can be separated, and both of the fragments are enzymatically inactive. If these fragments are then mixed, they recombine in equimolar amounts to reconstitute the active enzyme. It is possible that some genetic con- trol devices of the cell employ analogous mechanisms, in which the addi- tion or removal of a short peptide sequence determines enzyme activity. Only isolation and analysis of the enzyme in question could test this proposal. Information of the greatest importance about protein structure is com- ing from the incredibly complex and beautiful analysis of the tertiary structure of hemoglobin by means of X-ray crystallography. In these studies, atomic structure is observed by means of X-ray diffraction pat- terns which provide the raw data for calculating relative electron densi- r^ Treat with subtilizin u RNA-ase A 100% active which breaks one particular peptide bond. RNA-ase S 100% active. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original Sager, Ruth; Ryan, Francis J. (Francis Joseph), 1916-. New York, Wiley
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